The structure of a sulfated glycoprotein of chick allantoic fluid.

The molecular structure of a sulfated glycoprotein from chick chorioallantoic fluid has been investigated. The effect of alkali and alkali-borohydride under various conditions has been shown to lead to quantitatively and qualitatively different products of elimination and reduction. The carbohydrate chains of the products, by gel filtration, were heterogeneous, ranging from an average molecular weight of 1,100 to 2,600. The purified glycoprotein (mol wt 26,000 by gel filtration) contained a series of fatty acids bound to carbohydrate in ester linkage. The sialic acid of the glycoprotein was characterized as N-acetylneuraminic acid.